ID G5JFI0_9STAP Unreviewed; 381 AA.
AC G5JFI0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EHJ09053.1};
GN ORFNames=SS7213T_00961 {ECO:0000313|EMBL:EHJ09053.1};
OS Staphylococcus simiae CCM 7213 = CCUG 51256.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ09053.1, ECO:0000313|Proteomes:UP000005413};
RN [1] {ECO:0000313|EMBL:EHJ09053.1, ECO:0000313|Proteomes:UP000005413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ09053.1,
RC ECO:0000313|Proteomes:UP000005413};
RX PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT "Comparative genomic analysis of the genus Staphylococcus including
RT Staphylococcus aureus and its newly described sister species Staphylococcus
RT simiae.";
RL BMC Genomics 13:38-38(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ09053.1}.
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DR EMBL; AEUN01000019; EHJ09053.1; -; Genomic_DNA.
DR RefSeq; WP_002461751.1; NZ_AEUN01000019.1.
DR AlphaFoldDB; G5JFI0; -.
DR PATRIC; fig|911238.3.peg.175; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000005413; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 381 AA; 41526 MW; C7B3535621870C47 CRC64;
MKKKTKMIHG GHTTDDFTGA VTTPIYQTST YLQDDIGDLR QGYEYSRTAN PTRSSVESVI
AALENGKFGF AFSSGVAAIS AVVMLLDKGD HVILNSDVYG GTYRALTKVF TRFGIEVEFV
DTTNTDNIEQ AIKENTKMLF IETPSNPLLR VTDIKKSAEI AKQHHLISVV DNTFMTPYYQ
NPLDLGIDIV LHSATKYLGG HSDLVAGLVA TSDDDLAERL AFISNSTGGI LGPQDSYFLI
RGLKTLGLRM EQINRSVSDI IAMLQAHPAV QQVFHPSIES HLNHDVHVAQ ADGHTGVIAF
EVKDTDSAKQ VIRETEYYTL AESLGAVESL ISVPALMTHA SIPADIRAKE GITDGLVRIS
VGIEDTEDLV QDLKSALDTL K
//
